Alternating access mechanism in the POT family of oligopeptide transporters

• Nicolae Solcan ^[1] ; Jane Kwok ^[1] ; Philip W Fowler ^[1] ; Alexander D Cameron ^[3] ; David Drew ^[2] ; So Iwata ^[4] ; Simon Newstead ^[1]
  1. [1] University of Oxford

     University of Oxford

     Oxford District, Reino Unido

     
  2. [2] Imperial College London

     Imperial College London

     Reino Unido

     
  3. [3] Membrane Protein Laboratory, Diamond Light Source, Harwell Science and Innovation Campus, Didcot, UK; Research Complex at Harwell, Rutherford Appleton Laboratory, Didcot, UK; Division of Molecular Biosciences, Imperial College London, London, UK
  4. [4] Membrane Protein Laboratory, Diamond Light Source, Harwell Science and Innovation Campus, Didcot, UK; Research Complex at Harwell, Rutherford Appleton Laboratory, Didcot, UK; Division of Molecular Biosciences, Imperial College London, London, UK; Japan Science and Technology Agency, ERATO Human Receptor Crystallography Project, Kyoto, Japan; Japan Science and Technology Agency, ERATO Human Receptor Crystallography Project, Kyoto, Japan

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• Localización: EMBO journal: European Molecular Biology Organization, ISSN 0261-4189, Vol. 31, Nº. 16, 2012, págs. 3411-3421
• Idioma: inglés
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• Resumen

  • Proton-dependent oligopeptide transporters are required for the uptake of diet-derived peptides in all kingdoms of life. The crystal structure of a bacterial transporter in the inward open conformation, together with a published structure in an occluded conformation, reveals the peptide transport mechanism.